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Title: Thia fatty acids as substrates and inhibitors of stearoyl-CoA desaturase. Author: Høvik KE, Spydevold OS, Bremer J. Journal: Biochim Biophys Acta; 1997 Nov 30; 1349(3):251-6. PubMed ID: 9434139. Abstract: Thia fatty acids are fatty acid analogues, where sulfur atoms substitute methylene groups in the carbon chain. In 7800 C1 Morris hepatoma cells and in hepatocytes 9-thia and 10-thia stearic acid are strong inhibitors of stearoyl-Co desaturase, while 3,9-dithia stearic acid and 3,10-dithia stearic acid are much weaker inhibitors. No effect on the stearoyl-CoA desaturase can be observed with 3-thia stearic acid. In microsomes, an equimolar concentration of 9-thia stearoyl-CoA inhibits the delta9 desaturation of [1-14C]stearoyl-CoA approximately 75%, while 3,9-dithia stearoyl-CoA and 3,10-dithia stearoyl-CoA again are weak inhibitors. 3-Thia stearoyl-CoA has no effect on the desaturation of [1-14C]stearoyl-CoA. [2-14C]3-Thia stearoyl-CoA is delta9 desaturated to [2-14C]thia oleic acid. This desaturation is inhibited by unlabelled stearoyl-CoA, which therefore is the preferred substrate. These results show that a sulfur atom in the 3 position reduces the affinity of the CoA ester for the enzyme, but permits desaturation. A sulfur in the 9 or 10 position does not affect binding to the enzyme. The 9-thia and 10-thia stearoyl-CoA, which cannot be desaturated, therefore are strong inhibitors.[Abstract] [Full Text] [Related] [New Search]